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Significance NFAT5 mediates protection from adverse effects of hypertonicity. Cells, e.g. kidney, in hypertonic conditions take up salts and protective organic osmolytes. By mechanisms not fully understood, NFAT5 is activated and induces genes including those that code enzymes responsible for synthesizing protective osmolytes. We show that in solution the NFAT5 NTD, which contains one of NFAT5′s three transcription activation domains, undergoes hypertonicity- and/or osmolyte-induced disorder-to-order conformational rearrangement. In its more folded conformation, interaction of NFAT5 NTD with specific proteins is enhanced, including that with high mobility group protein (HMGI-C), which has been shown to protect against apoptosis. These findings suggest that in vivo, increased intracellular ionic strength, coupled with osmolytes, may directly activate NFAT5. They encourage further pursuit of this possibility.

NFAT5, which protects against hypertonicity, is activated by that stress via structuring of its intrinsically disordered domain